Cutting/adding/mutating residues at the termini is VERY OFTEN bad for the
folding. Keep in mind that oftentimes having extra residues is bad too. In
my field (crystallography) frequently the nature of the game is to find the
minimal-and-sufficient domain (or truncated protein) which will fold
correctly. It all depends on how much you cut - obviously if you remove a
residue that's crucial for folding your protein will not work out. We
routinely screen termini truncations for efficient folding and
crystallization.
A.G.E.
"Adrian" <AdrnLgrvtn at gazeta.pl> wrote in message
news:am8ge5$be7$1 at news.gazeta.pl...
> Have all positions along an amino acid sequence the potential to influence
> the folding equally importantly? Specificly, I wonder if amino acids
> positioned near both ends of a sequence could be crucial to how
3d-structure
> would look like? Whats more, will removing 1 or 2 aminoacids from a
> sequence's end (shortening) make any difference?
>> Kind Regards
> Adrian
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